ID   W9S8R4_9ROSA            Unreviewed;       827 AA.
AC   W9S8R4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=polyribonucleotide nucleotidyltransferase {ECO:0000256|ARBA:ARBA00012416};
DE            EC=2.7.7.8 {ECO:0000256|ARBA:ARBA00012416};
GN   ORFNames=L484_020536 {ECO:0000313|EMBL:EXC20316.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC20316.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC       family. {ECO:0000256|ARBA:ARBA00007404}.
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DR   EMBL; KE345913; EXC20316.1; -; Genomic_DNA.
DR   RefSeq; XP_010108801.1; XM_010110499.1.
DR   AlphaFoldDB; W9S8R4; -.
DR   STRING; 981085.W9S8R4; -.
DR   eggNOG; KOG1067; Eukaryota.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
DR   GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd11364; RNase_PH_PNPase_2; 1.
DR   Gene3D; 3.30.230.70; GHMP Kinase, N-terminal domain; 2.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012162; PNPase.
DR   InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR   InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR   InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR003029; S1_domain.
DR   NCBIfam; TIGR03591; polynuc_phos; 1.
DR   PANTHER; PTHR11252; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; 1.
DR   PANTHER; PTHR11252:SF0; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE 1, MITOCHONDRIAL; 1.
DR   Pfam; PF03726; PNPase; 1.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 2.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF46915; Polynucleotide phosphorylase/guanosine pentaphosphate synthase (PNPase/GPSI), domain 3; 1.
DR   SUPFAM; SSF55666; Ribonuclease PH domain 2-like; 2.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030645};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EXC20316.1}.
FT   DOMAIN          512..580
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          662..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..714
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   827 AA;  90359 MW;  D06079DC6E4A97C9 CRC64;
     MAANATSAAL MLSDIPWGGP IGMIRIGRIS GQFIVNPTMD ELCFSDLNLV YACTKDKTLM
     MDVQARGISE KDLEAGLRLA HPEMLDCDYL TIQAVKYLEP QIRLAAKAGK GKKDYKLSML
     SDRTLERVRE LAEAPIEAVF SDPTYGKFER GGALDNITQD VKKVLEEECD GESLNVLSKT
     VDTVRKQVVR RRIISEGLRV DGRRLDEVRP LYCEAGNLPQ LHGSSLFSRG DTQVLCTVTL
     GSPADAQRLD SIVGSSSKRF MLHYSFPPFC INEVGKRGGL NRREVGHGTL AEKALLAVLP
     PEDDFPYVVR INSEVMASDG STSMATVCGG SMALMDAGIS LREHVAGVSV GLVSEVDPST
     GKIKDYRILT DILGLEDHLG DMDFKIAGTR KGVTAIQLDI KPAGIPLDII CESLEHARKG
     RIQILDQMEK EINAPRDQDD NSPQLATLKY SNDLLRRLVG PLGALKRKIE EETGGRLSVS
     DGTLSIVAKN KAIMEKVKEK IDFLLGREIE IGGVYKGVVT SVKEYGAFVE FNGGQQGLLH
     ISELSHEPVS RPSEVVSVGQ KITAKCIGQD VRGNIKLSLK ATIPQSGSVK RNVAKASFPS
     SKEEVEYSAS EENMCNAGEK QNNITDTLDA FLVNKNEVSD VNPSQFSVPP ILIRSAAECD
     EEEKSAGLTE KSKTKSRSLG ASEADGKSKP SLRKKGDKRL NSKSKSKDGE EITQILKSDT
     SNRSNLDDSE AETRTTISAK SLKLGTKVTA KVFQVRTNGL ILDLGGDIRG MYLFESNEIL
     FNRVAKGPCV FMQTNGRRDF EEGDELRVQC TRFNRKGVPV MSLVDDD
//